6fao | pdb_00006fao

Discovery and characterization of a thermostable GH6 endoglucanase from a compost metagenome

spinqualitylabelsall models 6fao, resolution 1.88Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6fao is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, SO4 Activity: Cellulase, with EC number 3.2.1.4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Enzymatic depolymerization of recalcitrant polysaccharides plays a key role in accessing the renewable energy stored within lignocellulosic biomass, and natural biodiversities may be explored to discover microbial enzymes that have evolved to conquer this task in various environments. Here, a metagenome from a thermophilic microbial community was mined to yield a novel, thermostable cellulase, named mgCel6A, with activity on an industrial cellulosic substrate (sulfite-pulped Norway spruce) and a glucomannanase side activity. The enzyme consists of a glycoside hydrolase family 6 catalytic domain (GH6) and a family 2 carbohydrate binding module (CBM2) that are connected by a linker rich in prolines and threonines. MgCel6A exhibited maximum activity at 85 degrees C and pH 5.0 on carboxymethyl cellulose (CMC), but in prolonged incubations with the industrial substrate, the highest yields were obtained at 60 degrees C, pH 6.0. Differential scanning calorimetry (DSC) indicated a Tm(app) of 76 degrees C. Both functional data and the crystal structure, solved at 1.88 A resolution, indicate that mgCel6A is an endoglucanase. Comparative studies with a truncated variant of the enzyme showed that the CBM increases substrate binding, while not affecting thermal stability. Importantly, at higher substrate concentrations the full-length enzyme was outperformed by the catalytic domain alone, underpinning previous suggestions that CBMs may be less useful in high-consistency bioprocessing. Discovery and characterization of a thermostable two-domain GH6 endoglucanase from a compost metagenome.,Jensen MS, Fredriksen L, MacKenzie AK, Pope PB, Leiros I, Chylenski P, Williamson AK, Christopeit T, Ostby H, Vaaje-Kolstad G, Eijsink VGH PLoS One. 2018 May 24;13(5):e0197862. doi: 10.1371/journal.pone.0197862., eCollection 2018. PMID:29795644 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA